Mercury in PDB 1g45: Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2- Fluorophenyl)Methyl]-Benzamide

Enzymatic activity of Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2- Fluorophenyl)Methyl]-Benzamide

All present enzymatic activity of Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2- Fluorophenyl)Methyl]-Benzamide:
4.2.1.1;

Protein crystallography data

The structure of Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2- Fluorophenyl)Methyl]-Benzamide, PDB code: 1g45 was solved by C.-Y.Kim, J.S.Chang, J.B.Doyon, T.T.Baird Jr., C.A.Fierke, A.Jain, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	20.00 / 1.83
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	42.890, 41.920, 72.850, 90.00, 104.71, 90.00
*R / R_free (%)*	18.1 / 23.9

Other elements in 1g45:

The structure of Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2- Fluorophenyl)Methyl]-Benzamide also contains other interesting chemical elements:

Fluorine	(F)	1 atom
Zinc	(Zn)	1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2- Fluorophenyl)Methyl]-Benzamide (pdb code 1g45). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total only one binding site of Mercury was determined in the Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2- Fluorophenyl)Methyl]-Benzamide, PDB code: 1g45:

Mercury binding site 1 out of 1 in 1g45

Go back to

Mercury Binding Sites List in 1g45

Mercury binding site 1 out of 1 in the Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2- Fluorophenyl)Methyl]-Benzamide

Mono view

Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2- Fluorophenyl)Methyl]-Benzamide within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Hg263 b:48.1 occ:1.00	O	A:VAL135	3.0	26.0	1.0
	CB	A:CYS206	3.0	12.6	1.0
	O	A:GLN137	3.0	20.3	1.0
	C	A:GLN137	3.2	19.9	1.0
	N	A:GLN137	3.2	20.7	1.0
	C	A:GLN136	3.3	21.3	1.0
	O	A:GLU205	3.6	12.6	1.0
	CA	A:CYS206	3.6	11.2	1.0
	O	A:GLN136	3.7	20.2	1.0
	CA	A:GLN137	3.7	21.2	1.0
	C	A:VAL135	3.8	22.0	1.0
	CA	A:GLN136	3.8	21.5	1.0
	N	A:PRO138	3.8	18.8	1.0
	C	A:GLU205	3.9	10.3	1.0
	N	A:CYS206	3.9	11.9	1.0
	O	A:HOH306	3.9	19.9	1.0
	N	A:GLN136	4.2	21.0	1.0
	SG	A:CYS206	4.2	25.4	1.0
	CA	A:PRO138	4.2	17.3	1.0
	O	A:HOH301	4.5	24.7	1.0
	N	A:GLU205	4.7	8.5	1.0
	CD	A:PRO138	4.8	20.8	1.0
	O	A:ALA134	4.9	17.9	1.0
	CA	A:GLU205	4.9	8.8	1.0
	CA	A:VAL135	4.9	19.7	1.0

Reference:

C.-Y.Kim, J.S.Chang, J.B.Doyon, T.T.Baird Jr., C.A.Fierke, A.Jain, D.W.Christianson. Contribution of Flourine to Protein-Ligand Affinity in the Binding of Flouroaromatic Inhibitors to Carbonic Anhydrase II J.Am.Chem.Soc. V. 122 12125 2000.
ISSN: ISSN 0002-7863
DOI: 10.1021/JA002627N

Page generated: Sat Aug 10 23:47:03 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0

	© Copyright 2008-2020 by atomistry.com
Home \| Site Map \| Copyright \| Contact us \| Privacy